Abstract: Phosphorylation is a common protein modification by which a cell or virus regulates protein activity, and subsequently cellular and viral functions. Herpesviruses commonly encode protein kinases that regulate their own replicative processes and modify host cellular machinery, by phosphorylating target proteins. Although numerous studies have revealed the multiple downstream effects of viral protein kinases and their potential molecular mechanisms, it remains unknown whether herpes viral protein kinases are involved in viral replication and pathogenicity in vivo. This review focuses on Us3 protein kinase encoded by herpes simplex virus 1 and provides a current overview of its functions in infected cells, with a special focus on their relevancy in vivo.
*Division of Molecular Virology, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan; and
†Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Reprints: Yasushi Kawaguchi, Division of Molecular Virology, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan (e-mail: email@example.com).
Studies by the author in this review were supported by the Funding Program for Next Generation World-Leading Researchers and Grants for Scientific Research from the Japan Society for the Promotion of Science (JSPS), a contract research fund for the Program of Japan Initiative for Global Research Network on Infectious Diseases and Global COE Program “Center of Education and Research for the Advanced Genome-Based Medicine—For personalized medicine and the control of worldwide infectious diseases” from the Ministry of Education, Culture, Science, Sports and Technology (MEXT) of Japan, and grants from the Takeda Science Foundation and the Naito Foundation.
The author has no conflicts of interest to disclose.